Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin
Acidic proteins play an important role during mineral formation in biological systems, but the mechanism of mineral formation is far from understood. In this paper, we report on the relationship between the structure of a protein and hydroxyapatite deposition under biomimetic conditions. Sericin, a...
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Published in: | Journal of the Royal Society interface Vol. 2; no. 4; pp. 373 - 378 |
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Main Authors: | , , , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
London
The Royal Society
22-09-2005
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Subjects: | |
Online Access: | Get full text |
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Summary: | Acidic proteins play an important role during mineral formation in biological systems, but the mechanism of mineral formation is far from understood. In this paper, we report on the relationship between the structure of a protein and hydroxyapatite deposition under biomimetic conditions. Sericin, a type of silk protein, was adopted as a suitable protein for studying structural effect on hydroxyapatite deposition, since it forms a hydroxyapatite layer on its surface in a metastable calcium phosphate solution, and its structure has been reported. Sericin effectively induced hydroxyapatite nucleation when it has high molecular weight and a β sheet structure. This indicates that the specific structure of a protein can effectively induce heterogeneous nucleation of hydroxyapatite in a biomimetic solution, i.e. a metastable calcium phosphate solution. This finding is useful in understanding biomineralization, as well as for the design of organic polymers that can effectively induce hydroxyapatite nucleation. |
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Bibliography: | istex:C005116DA54001FFD9BB8D4CD1F483F294BC9996 ArticleID:rsif20050052 Author for correspondence ark:/67375/V84-R1T9MTDM-W href:373.pdf ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 1742-5689 1742-5662 |
DOI: | 10.1098/rsif.2005.0052 |